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| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | PNTx4 |
| Uniprot No | P59368 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-82aa |
| 氨基酸序列 | CGDINAACKEDCDCCGYTTACDCYWSKSCKCREAAIVIYTAPKKKLTC |
| 预测分子量 | 7.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下为示例性参考文献(注：PNTx4相关研究目前公开信息有限，以下内容为假设性示例，建议通过学术数据库核实具体文献)：
1. **标题**：Recombinant PNTx4 Expression and Neuroprotective Effects in a Mouse Model of Parkinson's Disease
**作者**：Chen L, et al.
**摘要**：研究利用大肠杆菌系统表达重组PNTx4蛋白，纯化后验证其抑制神经元凋亡的活性，并在帕金森模型小鼠中显示多巴胺能神经保护作用。
2. **标题**：Structural Characterization of PNTx4 Toxin from Phoneutria nigriventer Venom Using Cryo-EM
**作者**：Silva R, et al.
**摘要**：通过冷冻电镜解析PNTx4的三维结构，揭示其与电压门控钙通道结合的分子机制，为神经痛治疗药物开发提供依据。
3. **标题**：Optimization of PNTx4 Production in Pichia pastoris for Anticonvulsant Drug Development
**作者**：Kim J, et al.
**摘要**：优化毕赤酵母表达系统提高PNTx4产量，并证实重组蛋白在癫痫模型中延长惊厥潜伏期，具有潜在抗惊厥应用价值。
4. **标题**：PNTx4 Recombinant Protein Attenuates Neuroinflammation via TLR4/NF-κB Pathway Inhibition
**作者**：Gomez M, et al.
**摘要**：体外实验表明重组PNTx4通过调控TLR4/NF-κB信号通路降低小胶质细胞炎症因子释放，提示其治疗神经炎症疾病的潜力。
**建议**：可通过PubMed、Google Scholar等平台，以关键词“PNTx4 recombinant protein”或“Phoneutria toxin x4”检索最新文献，注意部分研究可能使用“PnTx4”缩写命名。
PNTx4 recombinant protein is a biologically active derivative of a neurotoxin originally isolated from the venom of *Phoneutria nigriventer*, commonly known as the Brazilian armed spider. This spider's venom contains a complex mixture of peptides, many of which target ion channels or receptors in the nervous system. PNTx4. in particular, is a small, cysteine-rich peptide that modulates voltage-gated sodium (NaV) and calcium (CaV) channels. Its recombinant form is produced via genetic engineering in heterologous expression systems (e.g., *E. coli* or yeast), ensuring scalability and purity for research or therapeutic applications.
The native PNTx4 toxin exhibits high affinity for neuronal ion channels, influencing membrane excitability and synaptic transmission. Studies suggest it may act as a partial inhibitor or modulator, depending on the channel subtype and cellular context. Recombinant PNTx4 retains these properties, making it a valuable tool for studying ion channel physiology, pain signaling pathways, and neurological disorders. Its structure includes disulfide bonds critical for stability and function, which are carefully preserved during recombinant production.
Research highlights its potential therapeutic relevance, particularly in pain management. By selectively targeting NaV channels involved in nociception, PNTx4 could offer alternatives to opioids with reduced side effects. Additionally, its calcium channel interactions may inform treatments for epilepsy or neurodegenerative conditions. However, challenges remain in optimizing delivery and specificity. Current work focuses on structure-activity relationships, toxicity profiling, and preclinical validation. As a recombinant product, PNTx4 exemplifies the intersection of toxinology and biotechnology, enabling precise exploration of venom-derived molecules for biomedical innovation.
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